scholarly journals Early events of secretory granule formation in the rat parotid acinar cell under the influence of isoproterenol. An ultrastructural and lectin cytochemical study

10.4081/1627 ◽  
2009 ◽  
Vol 45 (2) ◽  
pp. 169 ◽  
Author(s):  
F D’Amico ◽  
E Skarmoutsou ◽  
RM Imbesi ◽  
S Sanfilippo
Keyword(s):  
Secretory Granule ◽  
Acinar Cell ◽  
Granule Formation ◽  
Cytochemical Study ◽  
Parotid Acinar Cell ◽  
Rat Parotid

scholarly journals Interaction between zymogen granule and membrane of rat parotid acinar cell, in vitro.

1993 ◽  
Vol 61 ◽  
pp. 57
Author(s):  
Takahiro Nagao ◽  
Ritsuko Fujimoto ◽  
Hideaki Nishio ◽  
Fumiaki Hata
Keyword(s):  
Acinar Cell ◽  
Zymogen Granule ◽  
Parotid Acinar Cell ◽  
Rat Parotid

Morphological Effects of WR-2721 on the Rat Parotid Acinar Cell

1978 ◽  
Vol 75 (2) ◽  
pp. 327 ◽  
Author(s):  
N. E. Pratt ◽  
M. Sodicoff
Keyword(s):  
Acinar Cell ◽  
Parotid Acinar Cell ◽  
Rat Parotid

scholarly journals Uptake and fate of luminally administered horseradish peroxidase in resting and isoproterenol-stimulated rat parotid acinar cells.

1978 ◽  
Vol 76 (1) ◽  
pp. 207-229 ◽  
Author(s):  
C Oliver ◽  
A R Hand
Keyword(s):  
Horseradish Peroxidase ◽  
Secretory Granule ◽  
Extracellular Fluid ◽  
Acinar Cells ◽  
Granule Formation ◽  
Parotid Acinar Cells ◽  
Junctional Complexes ◽  
Rat Parotid ◽  
Endocytic Vesicles ◽  
Gain Access

The formation and fate of apical endocytic vesicles in resting and isoproterenol-stimulated rat parotid acinar cells were studied using luminally administered horseradish peroxidase (HRP) to mark the vesicles. The tracer was taken up from the lumen by endocytosis in small, smooth-surfaces "c"- or ring-shaped vesicles. About 1 h after HRP administration the vesicles could be found adjacent to the Golgi apparatus. At later times HRP reaction product was localized in multivesicular bodies and lysosomes; in isoproterenol-stimulated cells it was also present in autophagic vacuoles. HRP reaction product was never localized in any structure associated with secretory granule formation. These results suggest that the apical endocytic vesicles play a role in membrane recovery, but that they are degraded and not reutilized directly in secretory granule formation. Additionally, it was found that when isoproterenol was injected before HRP administration, the apical junctional complexes became permeable to the tracer, allowing it to gain access to the lateral and basal intercellular spaces. This permeability may provide an additional route whereby substances in the extracellular fluid could reach the saliva.

scholarly journals Effects of muscarinic, alpha-adrenergic, and substance P agonists and ionomycin on ion transport mechanisms in the rat parotid acinar cell. The dependence of ion transport on intracellular calcium.

1989 ◽  
Vol 93 (2) ◽  
pp. 285-319 ◽  
Author(s):  
S P Soltoff ◽  
M K McMillian ◽  
L C Cantley ◽  
E J Cragoe ◽  
B R Talamo
Keyword(s):  
Substance P ◽  
Ion Transport ◽  
Acinar Cell ◽  
Fluid Secretion ◽  
Ion Fluxes ◽  
Transport Systems ◽  
K Channel ◽  
Muscarinic Agonist ◽  
Parotid Acinar Cell ◽  
Rat Parotid

The relationship between receptor-mediated increases in the intracellular free calcium concentration [( Ca]i) and the stimulation of ion fluxes involved in fluid secretion was examined in the rat parotid acinar cell. Agonist-induced increases in [Ca]i caused the rapid net loss of up to 50-60% of the total content of intracellular chloride (Cli) and potassium (Ki), which is consistent with the activation of calcium-sensitive chloride and potassium channels. These ion movements were accompanied by a 25% reduction in the intracellular volume. The relative magnitudes of the losses of Ki and the net potassium fluxes promoted by carbachol (a muscarinic agonist), phenylephrine (an alpha-adrenergic agonist), and substance P were very similar to their characteristic effects on elevating [Ca]i. Carbachol stimulated the loss of Ki through multiple efflux pathways, including the large-conductance Ca-activated K channel. Carbachol and substance P increased the levels of intracellular sodium (Nai) to more than 2.5 times the normal level by stimulating the net uptake of sodium through multiple pathways; Na-K-2Cl cotransport accounted for greater than 50% of the influx, and approximately 20% was via Na-H exchange, which led to a net alkalinization of the cells. Ionomycin stimulated similar fluxes through these two pathways, but also promoted sodium influx through an additional pathway which was nearly equivalent in magnitude to the combined uptake through the other two pathways. The carbachol-induced increase in Nai and decrease in Ki stimulated the activity of the sodium pump, measured by the ouabain-sensitive rate of oxygen consumption, to nearly maximal levels. In the absence of extracellular calcium or in cells loaded with the calcium chelator BAPTA (bis[o-aminophenoxy]ethane-N,N,N',N'-tetraacetic acid) the magnitudes of agonist- or ionomycin-stimulated ion fluxes were greatly reduced. The parotid cells displayed a marked desensitization to substance P; within 10 min the elevation of [Ca]i and alterations in Ki, Nai, and cell volume spontaneously returned to near baseline levels. In addition to quantitating the activation of various ion flux pathways in the rat parotid acinar cell, these results demonstrate that the activation of ion transport systems responsible for fluid secretion in this tissue is closely linked to the elevation of [Ca]i.

Endotoxin can decrease isolated rat parotid acinar cell amylase secretion in a nitric oxide-independent manner

2005 ◽  
Vol 524 (1-3) ◽  
pp. 169-173 ◽  
Author(s):  
Adrienn Barta ◽  
Ildikó Tarján ◽  
Ágnes Kittel ◽  
Krisztina Horváth ◽  
Anikó Pósa ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Acinar Cell ◽  
Amylase Secretion ◽  
Independent Manner ◽  
Parotid Acinar Cell ◽  
Rat Parotid ◽  
Isolated Rat

Alpha-lactalbumin acts as a bimodal regulator of rat parotid acinar cell growth

1987 ◽  
Vol 147 (1) ◽  
pp. 174-181 ◽  
Author(s):  
Michael G. Humphreys-Beher ◽  
Charlotte A. Schneyer ◽  
Tivadar Zelles
Keyword(s):  
Cell Growth ◽  
Acinar Cell ◽  
Parotid Acinar Cell ◽  
Rat Parotid ◽  
Alpha Lactalbumin

scholarly journals Secretion of old versus new exportable protein in rat parotid slics. Control by neurotransmitters.

1976 ◽  
Vol 71 (1) ◽  
pp. 107-122 ◽  
Author(s):  
Y Sharoni ◽  
S Eimerl ◽  
M Schramm
Keyword(s):  
Acinar Cell ◽  
Adrenergic Receptor ◽  
Secretory Granules ◽  
Beta Adrenergic Receptor ◽  
Beta Adrenergic ◽  
Amylase Release ◽  
Chase Period ◽  
Parotid Acinar Cell ◽  
Rat Parotid

The possibility that old and new secretory granules do not mix and that older exportable protein can be secreted preferentially was tested on parotid gland in vitro. Slices from fasted animals were pulse labeled for 3 min with L-[3H]leucine. Subcellular fractionstion showed that after 1 90-min chase period, the formation of new labeled secretory granules was mostly completed. The ratio of label in secretory granules to label in microsomes increased 250-fold during the period 5--90 min postpulse. After the 90-min chase, a submaximal rate of secretion was initiated by adding a low concentration of isoproterenol to the slices. Preferential secretion of old unlabeled exportable protein was evident from the finding that the percent of total amylase secreted was 3.5-fold greater than the percent of labeled protein secreted. Preferential secretion of old unlabeled exportable amylase was undiminished even when the chase period before addition of isoproterenol was extended to 240 min. Such long chase incubations were still meaningful due to the fact that the spontaneous rat of amylase release and radioactive protein release from the slices was negligibly low. A high isoproterenol concentration added to the slices after a 90-min chase produced the following results. An initial phase of preferential secretion of old unlabeled protein was soon replaced by secretion of a random mixture of new and old exportable protein. Electron micrographs indicated that high rates of secretion involved sequential fusion of secretory granules so that the lumen extended deep into the cell where the new labeled granules were presumably located. At low rates of secretion, the lumen showed no such deep extensions. Experiments were also conducted on slices from glands which had been largely depleted of old granules by prior injection of isoproterenol into the animals. Secretion of labeled protein from such slices stopped with the export of 80% of the labeled protein. This finding indicates that about 20% of the radioactive protein is cellular nonexportable protein and that the slices are capable of exporting the entire amount of secretory protein which was symthesized in vitrol. In addition to the beta-adrenergic receptor which mediates protein secretion, the parotid acinar cell also possesses an alpha-adrenergic and a cholinergic receptor both of which cause K+ release, vacuole formation, and water secretion. Activation of either of the latter two receptors in conjunction with the beta-adrenergic receptor increased randomization of the protein secreted. It is concluded that in the rat parotid acinar cell there is little spontaneous mixing between old granules near the luminal cell membrane and new granules coming up behind from the Golgi complex. The neurotransmitters which induce secretion produce the observed randomization.

Development and characterization of SV40 immortalized rat parotid acinar cell lines

1998 ◽  
Vol 34 (1) ◽  
pp. 58-67 ◽  
Author(s):  
D. O. Quissell ◽  
K. A. Barzen ◽  
R. S. Redman ◽  
J. M. Camden ◽  
J. T. Turner
Keyword(s):  
Cell Lines ◽  
Acinar Cell ◽  
Parotid Acinar Cell ◽  
Rat Parotid

scholarly journals Rapid primary microwave-aldehyde and microwave-osmium fixation: improved detection of rat parotid acinar cell secretory granule alpha-amylase using a post-embedding immunogold ultrastructural morphometric analysis.

1995 ◽  
Vol 43 (5) ◽  
pp. 515-523 ◽  
Author(s):  
G R Login ◽  
T C Ku ◽  
A M Dvorak
Keyword(s):  
Salivary Gland ◽  
Secretory Granule ◽  
Acinar Cell ◽  
Alpha Amylase ◽  
Chemical Fixation ◽  
Thin Sections ◽  
Ultrastructural Studies ◽  
Rabbit Igg ◽  
Mw Irradiation ◽  
Rat Parotid

Studies of methods for improved fixation are becoming increasingly important in the field of quantitative immunocytochemistry. We used microwave (MW)-assisted chemical fixation to show improved retention of salivary gland acinar cell secretory granule alpha-amylase detected by a quantitative immunogold method. Blocks (4-mm3) of rat parotid gland were fixed by the following methods: (a) MW irradiation in an aldehyde fixative (AF) for 6 sec; (b) immersion in AF for 1.5 hr; (c) MW irradiation in osmium tetroxide (OT) for 9 sec; (d) immersion in OT for 1.5 hr; or (e) Sequential MW AF, 10 sec, MW OT rapid treatment (SMAORT), 10 sec. Specimens were processed routinely for transmission electron microscopy. Thin sections of Epon-embedded tissues were exposed first to rabbit IgG anti-human salivary alpha-amylase and second to gold-conjugated goat anti-rabbit IgG. Granule area was obtained by a point counting method. Labeling density was calculated as the number of gold particles/micron 2 +/- SD. Specimens fixed in seconds by MW-AF, MW-OT, or SMAORT showed ultrastructural preservation similar to immersion fixation in AF or OT for 1.5 hr. Immunogold labeling density of granule alpha-amylase was highest for SMAORT (874 microns 2) compared to MW-AF (295 microns 2), MW-OT (248 microns 2), routine sequential immersion in AF and OT (229 microns 2), or immersion in OT (no aldehyde) (190 microns 2). This study establishes the improved retention of salivary gland acinar cell secretory granule alpha-amylase and markedly enhanced fixation speed for ultrastructural studies made possible by MW-chemical fixation protocols that use aldehydes and osmium.

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